The 3C protease of picornaviruses is the subject of much interest, due to its central role in the infectivity of this family of viruses, which includes hepatitis A, poliomyelitis, and a number of rhinoviruses. These viruses are responsible for a number of human and animal diseases, such as the common cold and foot-and-mouth disease. Because structural knowledge of the active site of the 3C protease may provide information crucial to inhibitor design, a number of corporate drug-design groups have invested in such research, using both NMR and x-ray crystallography to solve 3C structures. Unfortunately, none of these results are availible to the general scientific community, due to the proprietary nature of this research. A collaboration with the Palmenberg lab on the Madison campus will allow the efficient generation of NMR quantities of labeled 3C protein from mengovirus. At this point, a protocol for purification of recombinant 3C (209 a.a.) overexpressed in E. coli has been developed, and milligram quantities of >90% pure protein have been produced. Current efforts are aimed at achieving high levels of expression in minimal media cultures and identifying appropriate solution conditions for NMR studies (i.e., buffer, pH, salt conc.). It is hoped that rapid progress toward structure determination will be made as soon as labeled protein is procured.